Before year 2000, it was generally assumed that the way in which proteins 'folded' was the sole key to understanding their function in life-systems. (See :Protein structuringplugin-autotooltip__plain plugin-autotooltip_bigProtein structuring

Genes set the order that amino acids (the chemical building blocks of proteins) appear in the proteins which they code for. But, working from the gene, the form which the protein's 3-D structure will take cannot as yet be predicted. The extremely complex shapes in which the protein 'folds' has a profound effect on the properties it has within an organism. ). Since then, it has been shown that many proteins do not entirely 'fold up' - leaving large sections of the protein chain as coils which appear to be random. This can profoundly affect the way in which they function and influence cellular systems.

It's currently estimated that around 33% of proteins found in cells which have a nucleus are 'Intrinsically Disordered'

It's largely unknown how the disordered sections might influence the proteins' function. Especially as, being unconstrained, they can re-organise and presumably operate in different ways at different times.

See: Wikipedia

Also see : Protein structuringplugin-autotooltip__plain plugin-autotooltip_bigProtein structuring

Genes set the order that amino acids (the chemical building blocks of proteins) appear in the proteins which they code for. But, working from the gene, the form which the protein's 3-D structure will take cannot as yet be predicted. The extremely complex shapes in which the protein 'folds' has a profound effect on the properties it has within an organism. and Protein Knottingplugin-autotooltip__plain plugin-autotooltip_bigProtein Knotting

Note: This article is an extension of the Protein Folding Problem

"Knotting in proteins was once considered exceedingly rare. However, systematic analyses of solved protein structures over the last two decades have demonstrated the existence of many deeply knotted proteins.